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Hepatitis B Virus e Antigen Physically Associates With Receptor-Interacting Serine/Threonine Protein Kinase 2 and Regulates IL-6 Gene Expression

Wu, Shuang ; Kanda, Tatsuo ; Imazeki, Fumio ; Nakamoto, Shingo ; Tanaka, Takeshi ; Arai, Makoto ; Roger, Thierry ; Shirasawa, Hiroshi ; Nomura, Fumio ; Yokosuka, Osamu

In: The Journal of Infectious Diseases, 2012, vol. 206, no. 3, p. 415-420

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    Titre
    • Hepatitis B Virus e Antigen Physically Associates With Receptor-Interacting Serine/Threonine Protein Kinase 2 and Regulates IL-6 Gene Expression
    Auteur
    • Wu, Shuang. Department of Medicine and Clinical Oncology
    • Kanda, Tatsuo. Department of Medicine and Clinical Oncology
    • Imazeki, Fumio. Department of Medicine and Clinical Oncology
    • Nakamoto, Shingo. Department of Medicine and Clinical Oncology
    • Tanaka, Takeshi. Department of Medicine and Clinical Oncology
    • Arai, Makoto. Department of Medicine and Clinical Oncology
    • Roger, Thierry. Infectious Diseases Service, Department of Medicine, Centre Hospitalier Universitaire Vaudois and University of Lausanne, Lausanne, Switzerland
    • Shirasawa, Hiroshi. Department of Molecular Virology
    • Nomura, Fumio. Department of Molecular Diagnosis, Graduate School of Medicine, Chiba University, Japan
    • Yokosuka, Osamu. Department of Medicine and Clinical Oncology
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • The Journal of Infectious Diseases, 2012, vol. 206, no. 3, p. 415-420. Oxford University Press
    Autre version électronique
    Classification
    • Santé
    Identifiant OAI-PMH
    • oai:doc.rero.ch:302306
    Summary
    We previously reported that hepatitis B virus (HBV) e antigen (HBeAg) inhibits production of interleukin 6 by suppressing NF-κB activation. NF-κB is known to be activated through receptor-interacting serine/threonine protein kinase 2 (RIPK2), and we examined the mechanisms of interleukin 6 regulation by HBeAg. HBeAg inhibits RIPK2 expression and interacts with RIPK2, which may represent 2 mechanisms through which HBeAg blocks nucleotide-binding oligomerization domain-containing protein 1 ligand-induced NF-κB activation in HepG2 cells. Our findings identified novel molecular mechanisms whereby HBeAg modulates intracellular signaling pathways by targeting RIPK2, supporting the concept that HBeAg could impair both innate and adaptive immune responses to promote chronic HBV infection